AROC1_SOLLC
ID AROC1_SOLLC Reviewed; 440 AA.
AC Q42884;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Chorismate synthase 1, chloroplastic;
DE EC=4.2.3.5;
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate phospholyase 1;
DE Flags: Precursor;
GN Name=CS1;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. UC82B;
RX PubMed=8251624; DOI=10.1007/bf00021526;
RA Goerlach J., Schmid J., Amrheim N.;
RT "Differential expression of tomato (Lycopersicon esculentum L.) genes
RT encoding shikimate pathway isoenzymes. II. Chorismate synthase.";
RL Plant Mol. Biol. 23:707-716(1993).
CC -!- FUNCTION: Catalyzes the last common step of the biosynthesis of
CC aromatic amino acids, produced via the shikimic acid pathway.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate +
CC phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5;
CC -!- COFACTOR:
CC Name=FMNH2; Xref=ChEBI:CHEBI:57618;
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 7/7.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in flowers and roots and,
CC to a lesser extent, in stems, leaves, and cotyledons.
CC -!- SIMILARITY: Belongs to the chorismate synthase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z21796; CAA79859.1; -; mRNA.
DR PIR; S40410; S40410.
DR RefSeq; NP_001234422.1; NM_001247493.2.
DR AlphaFoldDB; Q42884; -.
DR SMR; Q42884; -.
DR STRING; 4081.Solyc04g049350.2.1; -.
DR PaxDb; Q42884; -.
DR PRIDE; Q42884; -.
DR GeneID; 544154; -.
DR KEGG; sly:544154; -.
DR eggNOG; KOG4492; Eukaryota.
DR HOGENOM; CLU_034547_0_1_1; -.
DR InParanoid; Q42884; -.
DR OrthoDB; 826475at2759; -.
DR PhylomeDB; Q42884; -.
DR UniPathway; UPA00053; UER00090.
DR Proteomes; UP000004994; Unplaced.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004107; F:chorismate synthase activity; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IBA:GO_Central.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central.
DR CDD; cd07304; Chorismate_synthase; 1.
DR Gene3D; 3.60.150.10; -; 1.
DR HAMAP; MF_00300; Chorismate_synth; 1.
DR InterPro; IPR000453; Chorismate_synth.
DR InterPro; IPR035904; Chorismate_synth_AroC_sf.
DR InterPro; IPR020541; Chorismate_synthase_CS.
DR PANTHER; PTHR21085; PTHR21085; 1.
DR Pfam; PF01264; Chorismate_synt; 1.
DR SUPFAM; SSF103263; SSF103263; 1.
DR TIGRFAMs; TIGR00033; aroC; 1.
DR PROSITE; PS00787; CHORISMATE_SYNTHASE_1; 1.
DR PROSITE; PS00788; CHORISMATE_SYNTHASE_2; 1.
DR PROSITE; PS00789; CHORISMATE_SYNTHASE_3; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Chloroplast;
KW Lyase; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..54
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 55..440
FT /note="Chorismate synthase 1, chloroplastic"
FT /id="PRO_0000002296"
FT REGION 100..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 440 AA; 47722 MW; A4AFE9F410E2EAFA CRC64;
MASFVPTKQF VGASSSSDIG SSRLVSLQLP SKFSSSNFHL PSRPSQLKRL EIQAAGSTFG
NYFRVTTFGE SHGGGVGCII DGCPPRLPLS ESDMQVELDR RRPGQSRITT PRKETDTCKI
SSGTADGLTT GSPIKVEVPN TDQRGNDYSE MSLAYRPSHA DATYDFKYGV RSVQGGGRSS
ARETIGRVAA GAVAKKILKL YSGAEVLAYV SQVHQVVLPE DLIDHQNVTL EQIESNIVRC
PDPEYAEKMI AAIDAVRVRG DSVGGVVTCI VRNLPRGLGT PVFDKLEAEL AKACMSLPAT
KGFEFGSGFA GTFMTGSEHN DEFYMDEHGR IRTRTNRSGG IQGGISNGEV INMRIGFKPT
STISRKQQTV TRDKHETELI ARGRHDPCVV PRAVPMVEAM VALVLVDQLM AQYSQCMMFP
INPELQEPLQ SSPESAEVTL